Search results
Results from the WOW.Com Content Network
Needed for nerve cells, red blood cells, and to make DNA 6-14 × 10 −10: 1-10 × 10 −10: Cocarboxylase: 7-9 × 10 −8: Complement system: C1q 5.8-7.2 × 10 −5: C1r 2.5-3.8 × 10 −5: C1s (C1 esterase) 2.5-3.8 × 10 −5: C2 2.2-3.4 × 10 −5: C3( b1C-globulin) 8-15.5 × 10 −4: factor B (C3 proactivator) 2-4.5 × 10 −4: C4 (b1E ...
Red blood cells (RBCs), referred to as erythrocytes (from Ancient Greek erythros ' red ' and kytos ' hollow vessel ', with -cyte translated as 'cell' in modern usage) in academia and medical publishing, also known as red cells, [1] erythroid cells, and rarely haematids, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen (O 2) to the body tissues ...
A glycophorin is a sialoglycoprotein of the membrane of a red blood cell.It is a membrane-spanning protein and carries sugar molecules. It is heavily glycosylated (60%). Glycophorins are rich in sialic acid, which gives the red blood cells a very hydrophilic-charged
A:Normal red blood cells are shown flowing freely in a blood vessel on the top of the diagram. The inset image shows a cross-section of a normal red blood cell with normal hemoglobin. B:Demonstrates abnormal, sickled red blood cells blocking blood flow in a blood vessel (vaso-occlusive crisis). The inset image shows a cross-section of a sickle ...
Hemoglobin is an iron-containing protein that gives red blood cells their color and facilitates transportation of oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs to be exhaled. [3] Red blood cells are the most abundant cell in the blood, accounting for about 40–45% of its volume.
This page was last edited on 1 September 2003, at 10:36 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.
Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Protein 4.1 (80 kD) interacts with spectrin and short actin filaments to form the
Glycophorin C is the receptor for the protein erythrocyte binding antigen 140 (EBA140) of Plasmodium falciparum. [21] This interaction mediates a principal invasion pathway into the erythrocytes. The partial resistance of erythrocytes lacking this protein to invasion by P. falciparum was first noted in 1982. [ 22 ]